Contact order revisited: Influence of protein size on the folding rate
Contact order revisited: Influence of protein size on the folding rate
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DOI：
10.1110/ps.0302503
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发表时间：
2003-09-01
期刊：
影响因子：
8
通讯作者：
Finkelstein, AV
中科院分区：
文献类型：
--
作者：
Ivankov, DN;Garbuzynskiy, SO;Finkelstein, AV
基于最近成功建立的经验模型，通过蛋白质天然结构的相对接触顺序（CO）来预测小的两态折叠蛋白质的折叠速率；基于蛋白质折叠理论模型，预测折叠速率的对数随蛋白质链长L的减小而减小为L-2/3；基于发现多态折叠蛋白质的折叠速率与蛋白质的大小密切相关，而与CO的相关性很差，我们重新检查了折叠率对CO和L的依赖，试图找到一个结构参数，决定折叠率的蛋白质总量。我们发现，Abs_CO = CO x L能够相当准确地预测两态和多态折叠蛋白以及短肽的折叠率，并且该Abs_CO的蛋白质链长度为L0.70+/-0.07，所研究的单域蛋白和肽的总数。
Guided by the recent success of empirical model predicting the folding rates of small two-state folding proteins from the relative contact order (CO) of their native structures, by a theoretical model of protein folding that predicts that logarithm of the folding rate decreases with the protein chain length L as L-2/3, and by the finding that the folding rates of multistate folding proteins strongly correlate with their sizes and have very bad correlation with CO, we reexamined the dependence of folding rate on CO and L in attempt to find a structural parameter that determines folding rates for the totality of proteins. We show that the Abs_CO = CO x L, is able to predict rather accurately folding rates for both two-state and multistate folding proteins, as well as short peptides, and that this Abs-CO scales with the protein chain length as L0.70+/-0.07 for the totality of studied single-domain proteins and peptides.